Linked Life Data

15769619

Source:http://linkedlifedata.com/resource/pubmed/id/15769619

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-3-16
pubmed:abstractText
In the human genome, sequence analysis indicates there are five functional transmembrane guanylyl cyclases, enzymes that synthesize the intracellular second messenger, cGMP. Two, GC-A and GC-B or NPR-A and NPR-B, are widely distributed receptors for atrial natriuretic peptide, brain natriuretic peptide and C-type natriuretic peptide, more commonly known as ANP, BNP and CNP, respectively. One cyclase, GC-C or StaR, is predominantly found in the intestinal epithelium and is the receptor for guanylin and uroguanylin, as well as for the bacterial pathogen, heat-stable enterotoxin (Sta). The remaining two cyclases, GC-E and GC-F or RetGC-1 and RetGC-2, are expressed in the retina and regulate the dark cycle of phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. All five members consist of an extracellular ligand binding domain, single transmembrane spanning domain, and intracellular kinase homology, dimerization and guanylyl cyclase catalytic domains. In the first part of this review, the tissue expression, ligands and "knockout" phenotypes of each receptor are summarized and individual domains are compared. In the second part, regulation by ATP, calcium, protein kinase C and phosphorylation is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1205-20
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Domain analysis of human transmembrane guanylyl cyclase receptors: implications for regulation.
pubmed:affiliation
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 6-155 Jackson Hall, 321 Church Street, S. E., Minneapolis, USA. potter@umn.edu
pubmed:publicationType
Journal Article, Review